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- EMDB-67801: Setmelanotide bound to MC4R-Gq complex.Consensus refinement -

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Basic information

Entry
Database: EMDB / ID: EMD-67801
TitleSetmelanotide bound to MC4R-Gq complex.Consensus refinement
Map dataconsensus map
Sample
  • Complex: Cryo-EM structure of setmelanotide-bound human melanocortin receptor 4 in complex with Gq protein
Keywordshuman melanocortin receptor 4 / G protein-coupled receptor / setmelanotide / Gq / MEMBRANE PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.11 Å
AuthorsFeng WB
Funding support China, 6 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)82273961 China
National Natural Science Foundation of China (NSFC)82073904 China
National Natural Science Foundation of China (NSFC)81872915 China
Other government2021ZD0203400 China
Other governmentZDKJ2021028 China
Other government2024M762003 China
CitationJournal: Acta Pharm Sin B / Year: 2026
Title: Rationale of renewed efforts in developing MC4R modulators to treat metabolic disorders
Authors: Feng W / Zhou Q / Wang MW
History
DepositionDec 17, 2025-
Header (metadata) releaseAug 12, 2026-
Map releaseAug 12, 2026-
UpdateAug 12, 2026-
Current statusAug 12, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_67801.png

Downloads & links

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Map

FileDownload / File: emd_67801.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationconsensus map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.81 Å/pix.
x 256 pix.
= 207.36 Å		0.81 Å/pix.
x 256 pix.
= 207.36 Å		0.81 Å/pix.
x 256 pix.
= 207.36 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.81 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.9653745 - 1.3949683
Average (Standard dev.)-0.0009899668 (±0.028266836)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 207.36 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_67801_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_67801_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Cryo-EM structure of setmelanotide-bound human melanocortin recep...

EntireName: Cryo-EM structure of setmelanotide-bound human melanocortin receptor 4 in complex with Gq protein
Components
  • Complex: Cryo-EM structure of setmelanotide-bound human melanocortin receptor 4 in complex with Gq protein

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Supramolecule #1: Cryo-EM structure of setmelanotide-bound human melanocortin recep...

SupramoleculeName: Cryo-EM structure of setmelanotide-bound human melanocortin receptor 4 in complex with Gq protein
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 80.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.11 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 58767
Initial angle assignmentType: COMMON LINE
Final angle assignmentType: MAXIMUM LIKELIHOOD

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